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P24472

- GSTA4_MOUSE

UniProt

P24472 - GSTA4_MOUSE

Protein

Glutathione S-transferase A4

Gene

Gsta4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.1 Publication

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB

    GO - Biological processi

    1. glutathione metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase A4 (EC:2.5.1.18)
    Alternative name(s):
    GST A4-4
    Short name:
    GSTA4-4
    GST class-alpha member 4
    Glutathione S-transferase 5.7
    Short name:
    GST 5.7
    Gene namesi
    Name:Gsta4
    Synonyms:Gsta
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1309515. Gsta4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 222222Glutathione S-transferase A4PRO_0000185791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP24472.
    PaxDbiP24472.
    PRIDEiP24472.

    2D gel databases

    REPRODUCTION-2DPAGEP24472.

    PTM databases

    PhosphoSiteiP24472.

    Expressioni

    Gene expression databases

    BgeeiP24472.
    CleanExiMM_GSTA4.
    GenevestigatoriP24472.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP24472. 2 interactions.
    MINTiMINT-1487605.

    Structurei

    Secondary structure

    1
    222
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Turni14 – 163
    Helixi17 – 2610
    Beta strandi31 – 344
    Helixi38 – 458
    Turni46 – 483
    Beta strandi50 – 534
    Beta strandi57 – 604
    Beta strandi63 – 653
    Helixi68 – 7811
    Helixi86 – 10823
    Helixi109 – 1113
    Helixi114 – 13118
    Helixi133 – 14210
    Beta strandi145 – 1528
    Helixi155 – 16814
    Helixi174 – 1774
    Helixi179 – 18911
    Helixi192 – 1987
    Beta strandi199 – 2035
    Helixi210 – 21910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B48X-ray2.60A/B2-222[»]
    1GUKX-ray2.90A/B1-222[»]
    ProteinModelPortaliP24472.
    SMRiP24472. Positions 2-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24472.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8381GST N-terminalAdd
    BLAST
    Domaini85 – 208124GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 552Glutathione binding
    Regioni67 – 682Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Alpha family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiNOG266414.
    GeneTreeiENSGT00670000097856.
    HOGENOMiHOG000115734.
    HOVERGENiHBG053749.
    InParanoidiP24472.
    KOiK00799.
    OMAiMGMIMYL.
    OrthoDBiEOG79CZ0K.
    PhylomeDBiP24472.
    TreeFamiTF105321.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01266. GSTRNSFRASEA.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P24472-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAKPKLYYF NGRGRMESIR WLLAAAGVEF EEEFLETREQ YEKMQKDGHL    50
    LFGQVPLVEI DGMMLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ 100
    DLMMMIAVAP FKTPKEKEES YDLILSRAKT RYFPVFEKIL KDHGEAFLVG 150
    NQLSWADIQL LEAILMVEEL SAPVLSDFPL LQAFKTRISN IPTIKKFLQP 200
    GSQRKPPPDG PYVEVVRTVL KF 222
    Length:222
    Mass (Da):25,564
    Last modified:January 23, 2002 - v3
    Checksum:iB580E3415289424D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361E → D in BAB31640. (PubMed:16141072)Curated
    Sequence conflicti205 – 2062KP → SA in BAB27873. (PubMed:16141072)Curated
    Sequence conflicti218 – 2181T → I in AAA37754. (PubMed:1426286)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti115 – 1151K → P Requires 2 nucleotide substitutions.
    Natural varianti167 – 1671V → G.
    Natural varianti179 – 1802PL → GE.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06047 mRNA. Translation: AAA37754.1.
    AK008189 mRNA. Translation: BAB25520.1.
    AK008193 mRNA. Translation: BAB25524.1.
    AK008400 mRNA. Translation: BAB25649.1.
    AK008490 mRNA. Translation: BAB25696.1.
    AK009668 mRNA. Translation: BAB26429.1.
    AK010098 mRNA. Translation: BAB26701.1.
    AK011177 mRNA. Translation: BAB27449.1.
    AK011841 mRNA. Translation: BAB27873.1.
    AK019100 mRNA. Translation: BAB31546.1.
    AK019271 mRNA. Translation: BAB31640.1.
    BC012639 mRNA. Translation: AAH12639.1.
    CCDSiCCDS23357.1.
    PIRiS27234.
    RefSeqiNP_034487.2. NM_010357.3.
    UniGeneiMm.2662.

    Genome annotation databases

    EnsembliENSMUST00000034903; ENSMUSP00000034903; ENSMUSG00000032348.
    GeneIDi14860.
    KEGGimmu:14860.
    UCSCiuc009qty.2. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06047 mRNA. Translation: AAA37754.1 .
    AK008189 mRNA. Translation: BAB25520.1 .
    AK008193 mRNA. Translation: BAB25524.1 .
    AK008400 mRNA. Translation: BAB25649.1 .
    AK008490 mRNA. Translation: BAB25696.1 .
    AK009668 mRNA. Translation: BAB26429.1 .
    AK010098 mRNA. Translation: BAB26701.1 .
    AK011177 mRNA. Translation: BAB27449.1 .
    AK011841 mRNA. Translation: BAB27873.1 .
    AK019100 mRNA. Translation: BAB31546.1 .
    AK019271 mRNA. Translation: BAB31640.1 .
    BC012639 mRNA. Translation: AAH12639.1 .
    CCDSi CCDS23357.1.
    PIRi S27234.
    RefSeqi NP_034487.2. NM_010357.3.
    UniGenei Mm.2662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B48 X-ray 2.60 A/B 2-222 [» ]
    1GUK X-ray 2.90 A/B 1-222 [» ]
    ProteinModelPortali P24472.
    SMRi P24472. Positions 2-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P24472. 2 interactions.
    MINTi MINT-1487605.

    Chemistry

    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P24472.

    2D gel databases

    REPRODUCTION-2DPAGE P24472.

    Proteomic databases

    MaxQBi P24472.
    PaxDbi P24472.
    PRIDEi P24472.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034903 ; ENSMUSP00000034903 ; ENSMUSG00000032348 .
    GeneIDi 14860.
    KEGGi mmu:14860.
    UCSCi uc009qty.2. mouse.

    Organism-specific databases

    CTDi 2941.
    MGIi MGI:1309515. Gsta4.

    Phylogenomic databases

    eggNOGi NOG266414.
    GeneTreei ENSGT00670000097856.
    HOGENOMi HOG000115734.
    HOVERGENi HBG053749.
    InParanoidi P24472.
    KOi K00799.
    OMAi MGMIMYL.
    OrthoDBi EOG79CZ0K.
    PhylomeDBi P24472.
    TreeFami TF105321.

    Miscellaneous databases

    EvolutionaryTracei P24472.
    NextBioi 287101.
    PROi P24472.
    SOURCEi Search...

    Gene expression databases

    Bgeei P24472.
    CleanExi MM_GSTA4.
    Genevestigatori P24472.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01266. GSTRNSFRASEA.
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for mouse lung glutathione S-transferase GST 5.7."
      Zimniak P., Eckles M.A., Saxena M., Awasthi Y.C.
      FEBS Lett. 313:173-176(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo, Small intestine and Tongue.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Characterization of a novel glutathione S-transferase isoenzyme from mouse lung and liver having structural similarity to rat glutathione S-transferase 8-8."
      Medh R.D., Saxena M., Singhal S.S., Ahmad H., Awasthi Y.C.
      Biochem. J. 278:793-799(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 106-120 AND 167-184.
      Strain: CD-1.
      Tissue: Liver and Lung.
    5. "Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress."
      Krengel U., Schroter K.H., Hoier H., Arkema A., Kalk K.H., Zimniak P., Dijkstra B.W.
      FEBS Lett. 422:285-290(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
      Tissue: Lung.
    6. "Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface."
      Xiao B., Singh S.P., Nanduri B., Awasthi Y.C., Zimniak P., Ji X.
      Biochemistry 38:11887-11894(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
      Tissue: Lung.

    Entry informationi

    Entry nameiGSTA4_MOUSE
    AccessioniPrimary (citable) accession number: P24472
    Secondary accession number(s): Q9CQ81
    , Q9CTY7, Q9CY87, Q9D038
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    On the basis of immunological and kinetics data, GST 5.7 is distinct from alpha, mu and pI classes of GTS. However it has been postulated that this protein may be part of a distinct subgroup within this alpha class.
    The variations were found from AA sequencing and imply there are multiple forms of this protein. These variations are likely to be sex-linked and tissue specific.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3